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Conserved domains on  [gi|806638840|ref|NP_001292911|]
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bifunctional coenzyme A synthase precursor [Mus musculus]

Protein Classification

PPAT_CoAS and DPCK domain-containing protein( domain architecture ID 10114910)

PPAT_CoAS and DPCK domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 192-338 4.22e-66

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


:

Pssm-ID: 173915  Cd Length: 143  Bit Score: 211.37  E-value: 4.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 192 RGAVGGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDP 271
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638840 272 YGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDqshnENEEDKVSSSSFRQR 338
Cdd:cd02164   81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 359-535 1.30e-63

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


:

Pssm-ID: 238980  Cd Length: 179  Bit Score: 206.22  E-value: 1.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 359 VLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKI 438
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 439 LTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQM 518
Cdd:cd02022   81 LEAITHPLIRKEIEEQL--AEARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 806638840 519 SGQQLVEQSNVVLSTLW 535
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
 
Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 192-338 4.22e-66

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 211.37  E-value: 4.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 192 RGAVGGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDP 271
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638840 272 YGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDqshnENEEDKVSSSSFRQR 338
Cdd:cd02164   81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 359-535 1.30e-63

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 206.22  E-value: 1.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 359 VLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKI 438
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 439 LTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQM 518
Cdd:cd02022   81 LEAITHPLIRKEIEEQL--AEARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 806638840 519 SGQQLVEQSNVVLSTLW 535
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 358-551 5.73e-63

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 204.92  E-value: 5.73e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 358 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 437
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 438 ILTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 517
Cdd:COG0237   82 KLEAIVHPLVREEIERRL--AAARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 806638840 518 MSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLL 551
Cdd:COG0237  160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 358-531 7.79e-42

Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form Coenzyme A EC:2.7.1.24. This enzyme uses ATP in its reaction.


Pssm-ID: 426062  Cd Length: 180  Bit Score: 148.62  E-value: 7.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  358 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 437
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  438 ILTDIVWPVIAKLAREEmdVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 517
Cdd:pfam01121  81 WLNGILHPLIRREIFKQ--IATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158

                         170
                  ....*....|....
gi 806638840  518 MSGQQLVEQSNVVL 531
Cdd:pfam01121 159 ASREERLALADDVL 172
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 359-531 4.76e-36

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 133.28  E-value: 4.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  359 VLGLTGISGSGKSSVAQRLKNLGAY-IIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 437
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  438 ILTDIVWPVIAKLAREEMDVAVAKgKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 517
Cdd:TIGR00152  81 WLNALTHPLIRQWMKKLIAQFQSK-YALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRLASQ 159

                         170
                  ....*....|....
gi 806638840  518 MSGQQLVEQSNVVL 531
Cdd:TIGR00152 160 MDIEEKLARIDTVI 173
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 179-337 9.98e-35

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 128.91  E-value: 9.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 179 VARSPRQPVRGYHRGAVGGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPELLQPYAERVEHLTEFLVDIK 258
Cdd:PLN02388   8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638840 259 PSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDQSHNEneedKVSSSSFRQ 337
Cdd:PLN02388  88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPEESTGN----KLSSTTLRR 162
coaE PRK14734
dephospho-CoA kinase; Provisional
 357-555 5.13e-34

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 128.04  E-value: 5.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 357 LYVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQM 436
Cdd:PRK14734   1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 437 KILTDIVWPVIAKLAREEMDVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQS 516
Cdd:PRK14734  81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 806638840 517 QMSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLLQKRL 555
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 194-346 2.62e-31

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440642  Cd Length: 154  Bit Score: 118.76  E-value: 2.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 194 AVGGTFDRLHNAHKVLLSVACVLAqEQLVVGVADKDLLKsKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYG 273
Cdd:COG1019    5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 274 PAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKdqshneNEEDKVSSSSfrqRIL-------GNLLQP 346
Cdd:COG1019   83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL------AEDGKPISST---RIRngeidehGRLLKD 153
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 196-338 2.43e-11

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 61.57  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  196 GGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPelLQPYAERVEHLTEflvdIKPSLTFELVPLLDPYGPA 275
Cdd:pfam01467   3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638840  276 GSDPTLEFLVVSEETYRGgmAVNRFRLENGKEELAlyqIQLLKDQSHNENEEDKVSSSSFRQR 338
Cdd:pfam01467  77 LKELNPDVLVIGADSLLD--FWYELDEILGNVKLV---VVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 192-259 8.64e-05

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 40.75  E-value: 8.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638840  192 RGAVGGTFDRLHNAHKVLLSVACVLAqEQLVVGVAdKDLLKSKLLPELLQPYAERVEHLTEFLVDIKP 259
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 192-338 4.22e-66

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 211.37  E-value: 4.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 192 RGAVGGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDP 271
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638840 272 YGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDqshnENEEDKVSSSSFRQR 338
Cdd:cd02164   81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 359-535 1.30e-63

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 206.22  E-value: 1.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 359 VLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKI 438
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 439 LTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQM 518
Cdd:cd02022   81 LEAITHPLIRKEIEEQL--AEARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 806638840 519 SGQQLVEQSNVVLSTLW 535
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 358-551 5.73e-63

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 204.92  E-value: 5.73e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 358 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 437
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 438 ILTDIVWPVIAKLAREEMdvAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 517
Cdd:COG0237   82 KLEAIVHPLVREEIERRL--AAARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 806638840 518 MSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLL 551
Cdd:COG0237  160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 358-531 7.79e-42

Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form Coenzyme A EC:2.7.1.24. This enzyme uses ATP in its reaction.


Pssm-ID: 426062  Cd Length: 180  Bit Score: 148.62  E-value: 7.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  358 YVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 437
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  438 ILTDIVWPVIAKLAREEmdVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 517
Cdd:pfam01121  81 WLNGILHPLIRREIFKQ--IATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158

                         170
                  ....*....|....
gi 806638840  518 MSGQQLVEQSNVVL 531
Cdd:pfam01121 159 ASREERLALADDVL 172
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 359-531 4.76e-36

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 133.28  E-value: 4.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  359 VLGLTGISGSGKSSVAQRLKNLGAY-IIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 437
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  438 ILTDIVWPVIAKLAREEMDVAVAKgKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQ 517
Cdd:TIGR00152  81 WLNALTHPLIRQWMKKLIAQFQSK-YALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRLASQ 159

                         170
                  ....*....|....
gi 806638840  518 MSGQQLVEQSNVVL 531
Cdd:TIGR00152 160 MDIEEKLARIDTVI 173
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 179-337 9.98e-35

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 128.91  E-value: 9.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 179 VARSPRQPVRGYHRGAVGGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPELLQPYAERVEHLTEFLVDIK 258
Cdd:PLN02388   8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 806638840 259 PSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDQSHNEneedKVSSSSFRQ 337
Cdd:PLN02388  88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPEESTGN----KLSSTTLRR 162
coaE PRK14734
dephospho-CoA kinase; Provisional
 357-555 5.13e-34

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 128.04  E-value: 5.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 357 LYVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQM 436
Cdd:PRK14734   1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 437 KILTDIVWPVIAKLAREEMDVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQS 516
Cdd:PRK14734  81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 806638840 517 QMSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLLQKRL 555
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
coaE PRK03333
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
 360-549 2.07e-31

dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional


Pssm-ID: 179560 [Multi-domain]  Cd Length: 395  Bit Score: 125.89  E-value: 2.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 360 LGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKIL 439
Cdd:PRK03333   4 IGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALAAKAFADDEARAVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 440 TDIVWPVIAklAREEMDVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQMS 519
Cdd:PRK03333  84 NGIVHPLVG--ARRAELIAAAPEDAVVVEDIPLLVESGMAPLFHLVVVVDADVEVRVRRLVEQRGMAEADARARIAAQAS 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 806638840 520 GQQLVEQSNVVLSTLWESHVTQSQVEKAWN 549
Cdd:PRK03333 162 DEQRRAVADVWLDNSGTPDELVEAVRALWA 191
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 194-346 2.62e-31

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440642  Cd Length: 154  Bit Score: 118.76  E-value: 2.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 194 AVGGTFDRLHNAHKVLLSVACVLAqEQLVVGVADKDLLKsKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYG 273
Cdd:COG1019    5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 274 PAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKdqshneNEEDKVSSSSfrqRIL-------GNLLQP 346
Cdd:COG1019   83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL------AEDGKPISST---RIRngeidehGRLLKD 153
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
190-347 4.31e-28

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 109.54  E-value: 4.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 190 YHRGAVGGTFDRLHNAHKVLLSVACVLAQEqLVVGVADKDLLKSKLlPELLQPYAERVEHLTEFLVDIKPSLTFELVPLL 269
Cdd:PRK00777   1 MMKVAVGGTFDPLHDGHRALLRKAFELGKR-VTIGLTSDEFAKSYK-KHKVRPYEVRLKNLKKFLKAVEYDREYEIVKID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 270 DPYGPAGSDPtLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDqshneneEDKVSSSSFRQR-----ILGNLL 344
Cdd:PRK00777  79 DPYGPALEDD-FDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLA-------EDGKPISSTRIRrgeidEHGNLI 150


                 ...
gi 806638840 345 QPP 347
Cdd:PRK00777 151 KER 153
PLN02422 PLN02422
dephospho-CoA kinase
 359-546 4.89e-25

dephospho-CoA kinase


Pssm-ID: 215232  Cd Length: 232  Bit Score: 103.67  E-value: 4.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 359 VLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKI 438
Cdd:PLN02422   3 VVGLTGGIASGKSTVSNLFKSSGIPVVDADKVARDVLKKGSGGWKRVVAAFGEDILLPDGEVDREKLGQIVFSDPSKRQL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 439 LTDIVWPVIAKLAREEMDVAVAKGKTLCVIDAAMLLEAG---WQSMVHEVWtvVIPETEaVRRIVERDGLSEAAAQSRLQ 515
Cdd:PLN02422  83 LNRLLAPYISSGIFWEILKLWLKGCKVIVLDIPLLFETKmdkWTKPVVVVW--VDPETQ-LERLMARDGLSEEQARNRIN 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 806638840 516 SQMSGQQLVEQSNVVLSTLWESHVTQSQVEK 546
Cdd:PLN02422 160 AQMPLDWKRSKADIVIDNSGSLEDLKQQFQK 190
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
195-314 1.01e-12

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 69.46  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 195 VGGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPellQPYAERVEHLTEFLvdIKPSLTFELVPLLDPYGP 274
Cdd:PRK01170   5 VGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYP---IPYEDRKRKLENFI--KKFTNKFRIRPIDDRYGN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 806638840 275 AGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQI 314
Cdd:PRK01170  80 TLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLKIVRV 119
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 196-338 2.43e-11

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 61.57  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  196 GGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPelLQPYAERVEHLTEflvdIKPSLTFELVPLLDPYGPA 275
Cdd:pfam01467   3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 806638840  276 GSDPTLEFLVVSEETYRGgmAVNRFRLENGKEELAlyqIQLLKDQSHNENEEDKVSSSSFRQR 338
Cdd:pfam01467  77 LKELNPDVLVIGADSLLD--FWYELDEILGNVKLV---VVVRPVFFIPLKPTNGISSTDIRER 134
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 192-338 2.41e-08

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 53.21  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 192 RGAVGGTFDRLHNAHKVLLSVACVLAQEQLVVGVadKDLLKSKLLPELLQPYAERVEHLTEFLVDIKpsltfELVPLLDP 271
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIII--VSNPPKKKRNKDPFSLHERVEMLKEILKDRL-----KVVPVDFP 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 806638840 272 YGPAGSDPTL----------EFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDQShneneedKVSSSSFRQR 338
Cdd:cd02039   74 EVKILLAVVFilkillkvgpDKVVVGEDFAFGKNASYNKDLKELFLDIEIVEVPRVRDGK-------KISSTLIREL 143
PTZ00451 PTZ00451
dephospho-CoA kinase; Provisional
 359-519 2.45e-08

dephospho-CoA kinase; Provisional


Pssm-ID: 185630  Cd Length: 244  Bit Score: 54.88  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 359 VLGLTGISGSGKSSVAQRLKN-LGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMK 437
Cdd:PTZ00451   3 LIGLTGGIACGKSTVSRILREeHHIEVIDADLVVRELQAPNMACTRKIAARWPLCVHPETGELNRAELGKIIFSDAQARR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 438 ILTDIVWPVIAKLAREEMDVA---------VAKGKTLCVIDAAMLLEAG-WQSMVHEVWTVVIPETEAVRRIVERDGLSE 507
Cdd:PTZ00451  83 ALGRIMNPPIFRAILKRIAAAwwedlwrsgAGSSPLIVVLDAPTLFETKtFTYFVSASVVVSCSEERQIERLRKRNGFSK 162

                        170
                 ....*....|..
gi 806638840 508 AAAQSRLQSQMS 519
Cdd:PTZ00451 163 EEALQRIGSQMP 174
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 192-259 8.64e-05

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 40.75  E-value: 8.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806638840  192 RGAVGGTFDRLHNAHKVLLSVACVLAqEQLVVGVAdKDLLKSKLLPELLQPYAERVEHLTEFLVDIKP 259
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
COG4639 COG4639
Predicted kinase [General function prediction only];
362-503 4.98e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.58  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840 362 LTGISGSGKSSVAQRLkNLGAYIIDSDHLghRAyapggpayqpvveafgtdILHKDGTINRkvlgsrvfgnkkqmkiltd 441
Cdd:COG4639    7 LIGLPGSGKSTFARRL-FAPTEVVSSDDI--RA------------------LLGGDENDQS------------------- 46

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 806638840 442 iVWPVIAKLAREEMDVAVAKGKTLcVIDA--------AMLLEAGWQsmvHEVWTVVI----PETEAVRRIVERD 503
Cdd:COG4639   47 -AWGDVFQLAHEIARARLRAGRLT-VVDAtnlqrearRRLLALARA---YGALVVAVvldvPLEVCLARNAARD 115
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 359-388 8.84e-04

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 40.46  E-value: 8.84e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 806638840 359 VLGLTGISGSGKSSVA----QRLKNLG--AYIIDSD 388
Cdd:COG0529   18 VVWFTGLSGSGKSTLAnaleRRLFERGrhVYLLDGD 53
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 364-502 9.01e-04

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 39.99  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806638840  364 GISGSGKSSVAQRL-KNLGAYIIDSD--HLGHRAYAPGGPAYQPvveafgtdilhkdgtinrkvlgsrvfgnkkqmkILT 440
Cdd:pfam13671   6 GLPGSGKSTLARRLlEELGAVRLSSDdeRKRLFGEGRPSISYYT---------------------------------DAT 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 806638840  441 DIVWPVIAKLAREemdvaVAKGKTLCVIDAAMLLEAGWQSMV-----HEVWTVVI----PETEAVRRIVER 502
Cdd:pfam13671  53 DRTYERLHELARI-----ALRAGRPVILDATNLRRDERARLLalareYGVPVRIVvfeaPEEVLRERLAAR 118
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
357-408 1.45e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.51  E-value: 1.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 806638840 357 LYVLGltGISGSGKSSVAQRL-KNLGAYIIDSDHLGHRAYAPGGPAYQPVVEA 408
Cdd:COG0645    1 LILVC--GLPGSGKSTLARALaERLGAVRLRSDVVRKRLFGAGLAPLERSPEA 51
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 359-392 2.01e-03

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 41.07  E-value: 2.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 806638840 359 VLGLTGISGSGKSSVA----QRLKNLG--AYIIDSDHLGH 392
Cdd:PRK05506 462 TVWFTGLSGSGKSTIAnlveRRLHALGrhTYLLDGDNVRH 501
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 357-394 7.49e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 37.23  E-value: 7.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 806638840 357 LYVLglTGISGSGKSSVAQRL-KNLGAYIIDSDHLGHRA 394
Cdd:cd02021    1 IIVV--MGVSGSGKSTVGKALaERLGAPFIDGDDLHPPA 37
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 362-390 7.69e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 37.15  E-value: 7.69e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 806638840 362 LTGISGSGKSSVAQRL-KNLGAYIIDSDHL 390
Cdd:cd00464    4 LIGMMGAGKTTVGRLLaKALGLPFVDLDEL 33
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 358-392 8.77e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 37.61  E-value: 8.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 806638840 358 YVLGLTGISGSGKSSVA----QRLKNLG--AYIIDSDHLGH 392
Cdd:PRK03846  25 VVLWFTGLSGSGKSTVAgaleEALHELGvsTYLLDGDNVRH 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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